Odorant Binding to Bovine Odorant Binding Protein Detected by Intrinsic Fluorescence

Odorant binding to bovine odorant binding protein (OBPb) made OBPb structure a little tighter and odorant detection by intrinsic fluorescence possible. For odorant with high affinity such as 3,7-dimethyl-1-octanol (DMO), the binding reaction proceeded in a two-step manner that inferred an existence...

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Bibliographic Details
Published in:Chemistry letters 2005-09, Vol.34 (9), p.1256-1257
Main Authors: Ikematsu, Mineo, Takaoka, Daizo, Yasuda, Masashi
Format: Article
Language:English
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Summary:Odorant binding to bovine odorant binding protein (OBPb) made OBPb structure a little tighter and odorant detection by intrinsic fluorescence possible. For odorant with high affinity such as 3,7-dimethyl-1-octanol (DMO), the binding reaction proceeded in a two-step manner that inferred an existence of a third binding site.
ISSN:0366-7022
1348-0715
DOI:10.1246/cl.2005.1256